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Bio I USF Chapter 5 NOTES

by: Marla Notetaker

Bio I USF Chapter 5 NOTES BSC 2010

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Marla Notetaker

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This is the notes that I personally took from my reading on ch 5. I highlighted the key terms and vocabulary
Biology I Cellular Processes
Dr. Eric M. Sikorski
Class Notes
Proteins, Carbohydrates, sugars, DNA, RNA, nucleotides, phospholipids, saturated, hydrolsys, Macromolecules
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This 4 page Class Notes was uploaded by Marla Notetaker on Wednesday September 7, 2016. The Class Notes belongs to BSC 2010 at University of South Florida taught by Dr. Eric M. Sikorski in Fall 2016. Since its upload, it has received 57 views. For similar materials see Biology I Cellular Processes in Biology at University of South Florida.

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Date Created: 09/07/16
Chapter 5 – The Structure and Function of Large Biological Molecules Yellow: Vocabulary GREE: Key concepts  Macromolecules: carbohydrates, proteins, nucleic acids.  I. The Synthesis and Breakdown of Polymers  Enzymes: facilitate process of protein breakdown by acting as catalysis.  Dehydration: happens when 2 molecules SYNTHESIZE­ the molecules have  +          backbones of hydroxyl (OH ) and Hydrogen (H ) and to unite both           monomers a covalent bond is formed    Hydrolysis: used to break bonds between monomers by adding water the        compound, breaking the water molecule. Concept 5.2  Carbohydrates: includes monosaccharides and polymers of sugar. I. Sugars  Molecular formulas of the empirical formula CH O 2  Carbonyl: CO  Classifications of Carbon Skeletons: ­ Aldoses (Aldehyde Sugars): Carbonyl group at END of carbon skeleton ­ Ketoses (Ketone Sugars): Carbonyl groups WITHIN carbon skeleton ­ Trioses: 3­carbon sugars (C H O ) 3 6 3 ­ Pentose: 5­carbon sugars (C H O5) 10 5 ­ Hexoses: 6­carbon sugars (C H O 6 –12r6sent mostly in rings ­ Linear: carbons form in a straight line ­ Ring: carbon molecules are arranged in a ring.  Disaccharides: 2 monosaccharides joined by glycosidic linkage (a covalent bond             formed between 2 monosaccharides by dehydration). * Most prevalent sugar is SUCROSE – table sugar – made of  glucose (6C) and fructose (5C)* II. Polysaccharides  Are macromolecules, polymers with a few hundred to a few thousands  monosaccharides joined by glycosidic linkage. a. Storage Polysaccharides  Starch: polymer of glucose monomers – alpha glucose ­ Amylose: simplest form of starch… unbranched… 1­4 linkage ­ Amylopectin: complex form of starch… branched… 1­6 linkage (bended shape)  Glycogen: like Amylopectin but more extensively branches *Mainly in liver and muscle cells* b. Structural polysaccharides   Cellulose: major component of the cell wall of plants – the most abundant      organic compound on earth  ­ Beta glucose ­ They do not branch ­ Allow for hydrogen bonding   Chitin: the carbohydrate used by arthropods (insects) to build their exoskeletons.  (beta cellulose) Concept 5.3  Lipids: generally not large enough to be considereda macromolecule I. Fats  Made of: ­ Glycerol: is an alcohol which has 3 carbons with a hydroxyl group each ­ Fatty acids: long (abt 16­18 carbons) with a Carboxyl (COOH) backbone –  which is why is an acid. The rest of the chain is hydrocarbons.  Ester linkage:  dehydration reaction between the carboxyl group of the fatty acid                          and the hydroxyl group of the glycerol  Triacylglycerol (triglyceride): 3 fatty acids and 1 glycerol 1/02/lipids.html  Types of fats: ­ Saturated: as many hydrogen as possible are bound to carbon and there is no  double bonds to any carbon * Because it has no bends it’s flexible and allows the fat to      fold in itself.* ­ Unsaturated: there is at least one double bond of carbon * Hydrogenated vegetable oil refers to naturally unsaturated     fats that had been synthetically saturated by adding hydrogens*6 ­ Polyunsaturated: more than one double bond of carbon. ­ Trans fat: hydrogenating vegetable oil.  Uses: ­ Fats are mainly used to store energy ­ Serves as cushion to another organs (like the kidneys) ­ The subcutaneous adipose tissue (fat) serves to insulate the body. II. Phospholipids  Major factor in membranes  Has one 2 fatty acids with glycerol  The 3  Glycerol is tied to a phosphate group (PO ) 4  Behavior: ­ The hydrocarbons in one end are hydrophobic because they are NOT polar ­ The other end of it the phosphate has a negative charge therefore its hydrophilic. ­ When dropped into the water all the hydrophobic tails kind of arrange together  so the polar heads are facing the water creating a double layer (bilayer) III. Steroids  Carbon skeletons consisting of 4 fused rings  Cholesterol: ­ Important to membranes ­ In vertebrates... its stored in the liver and acquired from the diet Concept 5.4  Catalysts: chemical agents that selectively speeds up chemical reactions without being consumed by  the reaction  Polypeptide: polymers of peptides of amino acids  Protein: polypeptides, each folded and coiled into a specific three­dimensional structure  I. Amino Acid Monomers  An organic molecules with both an amino group and a carboxyl group (NH CHRCOOH)2  Alpha carbon: the carbon RIGHT IN THE MIDDLE of the amino acid… the one   attached to the R group.  There are 20 amino acids to code for all the proteins II. Polypeptides (Amino Acid Polymers)  Peptide bond: occurs to link 2 amino acids together so that one side (Amino group) is    next to the Carboxyl group and by process of dehydration. *SHAPE DETERMINES FUNCTION* a. 4 Levels of Protein Structure ­ Primary Structure: sequence of amino acids, long chain, codification ­ Secondary Structure: coils and folds by hydrogen bonds by backbones  Alpha helix: connected by hydrogen bonds every 4 AA *alpha­keratin: structural protein of hair*  Beta pleated sheet: 2 or more segments of the polypeptide       chain lying side by side (beta strands) are      connected by hydrogen bonds. *Silk protein of spider webs* *INTERACTIONS OF THE BACKBONES* ­ Tertiary Structure: overall shape of the interactions R groups – 3D shape  Hydrophobic interactions: polypeptides form their cluster      and the nonpolar hydrophilic part      of the peptide ends up in the core      of the protein leaving hydrophilic      part of the protein is free to      interact with other molecules with     hydrogen bonds and Van Der      Waals interactions keep the      hydrophobic portion together.  Disulfide Bridges: forms where 2 cysteine monomers (with      sulfhydryl – SH) and when the 2      monomers are brought together the 2      sulfurs are attracted to each other and they     bond, further reinforcing the shape of the      protein. ­ Quaternary Structure: polypeptides put together… the final protein   Collagen: 40% of human body  Hemoglobin: Oxygen binding  b. Sickle­Cell Disease: substitution of one amino acid (valine Val) for the normal  (glutamic acid Glu) *DENATURALIZATION: when the protein unfolds c. Protein folding in the cell ­ Chaperonins: protein molecules that assist in the proper folding of other proteins ­ X­ray Crystallography: used to determine the 3D shape of proteins. ­ Nuclear Magnetic Resonance Spectroscopy:  Concept 5.5  Gene: amino acid sequence of a polypeptide  Nucleic Acids: made of monomers of nucleotides I. The Roles of Nucleic Acids: gene expression – creating new proteins   Has 3 parts: ­ Nitrogenous base ­ Sugar ­ Phosphate  Deoxyribonucleic acid (DNA): genetic material inherited from parents, provides              directions for the replication – in 2­C it has H ­ Consists in 4 Bases o Pyrimidines – ONE ring with 6­membered  Cytosine (C)  Thymine (T in DNA)  Uracil (U in RNA) o Purines – ONE 6­membered ring AND 5­membered ring  Adenine (A)  Guanine (G)  Ribonucleic acid (RNA): controls protein synthesis in the ribosomes – in 2­C has OH II. The Components of Nucleic Acids  Polynucleotides: Polymers of nucleic acids  Nucleoside: nucleotide without the phosphate part http://watson­­and­ nucleotide/


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